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Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate

A(10)K (A=alanine, K=lysine) model peptides self‐assemble into ribbon‐like β‐sheet aggregates. Here, we report an X‐ray diffraction investigation on a flow‐aligned dispersion of these self‐assembly structures. The two‐dimensional wide‐angle X‐ray scattering pattern suggests that peptide pack in a tw...

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Autores principales: Kuczera, Stefan, Rüter, Axel, Roger, Kevin, Olsson, Ulf
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7496194/
https://www.ncbi.nlm.nih.gov/pubmed/32573909
http://dx.doi.org/10.1002/cphc.201901126
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author Kuczera, Stefan
Rüter, Axel
Roger, Kevin
Olsson, Ulf
author_facet Kuczera, Stefan
Rüter, Axel
Roger, Kevin
Olsson, Ulf
author_sort Kuczera, Stefan
collection PubMed
description A(10)K (A=alanine, K=lysine) model peptides self‐assemble into ribbon‐like β‐sheet aggregates. Here, we report an X‐ray diffraction investigation on a flow‐aligned dispersion of these self‐assembly structures. The two‐dimensional wide‐angle X‐ray scattering pattern suggests that peptide pack in a two‐dimensional oblique lattice, essentially identical to the crystalline packing of polyalanine, A(n) (for n>4). One side of the oblique unit cell, corresponding to the anti‐parallel β‐sheet, is oriented along the ribbon's axis. Together with recently published small angle X‐ray scattering data of the same system, this work thus yields a detailed description of the self‐assembled ribbon aggregates, down to the molecular length scale. Notably, our results highlight the importance of the crystalline peptide packing within its self‐assembly aggregates, which is often neglected.
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spelling pubmed-74961942020-09-25 Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate Kuczera, Stefan Rüter, Axel Roger, Kevin Olsson, Ulf Chemphyschem Communications A(10)K (A=alanine, K=lysine) model peptides self‐assemble into ribbon‐like β‐sheet aggregates. Here, we report an X‐ray diffraction investigation on a flow‐aligned dispersion of these self‐assembly structures. The two‐dimensional wide‐angle X‐ray scattering pattern suggests that peptide pack in a two‐dimensional oblique lattice, essentially identical to the crystalline packing of polyalanine, A(n) (for n>4). One side of the oblique unit cell, corresponding to the anti‐parallel β‐sheet, is oriented along the ribbon's axis. Together with recently published small angle X‐ray scattering data of the same system, this work thus yields a detailed description of the self‐assembled ribbon aggregates, down to the molecular length scale. Notably, our results highlight the importance of the crystalline peptide packing within its self‐assembly aggregates, which is often neglected. John Wiley and Sons Inc. 2020-06-23 2020-07-17 /pmc/articles/PMC7496194/ /pubmed/32573909 http://dx.doi.org/10.1002/cphc.201901126 Text en © 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.
spellingShingle Communications
Kuczera, Stefan
Rüter, Axel
Roger, Kevin
Olsson, Ulf
Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate
title Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate
title_full Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate
title_fullStr Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate
title_full_unstemmed Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate
title_short Two Dimensional Oblique Molecular Packing within a Model Peptide Ribbon Aggregate
title_sort two dimensional oblique molecular packing within a model peptide ribbon aggregate
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7496194/
https://www.ncbi.nlm.nih.gov/pubmed/32573909
http://dx.doi.org/10.1002/cphc.201901126
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